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P09826 (GLNA1_RHILV) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamine synthetase 1

EC=6.3.1.2
Alternative name(s):
Glutamate--ammonia ligase I
Glutamine synthetase I
Short name=GSI
Gene names
Name:glnA
OrganismRhizobium leguminosarum bv. viciae
Taxonomic identifier387 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupRhizobium

Protein attributes

Sequence length469 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

ATP + L-glutamate + NH3 = ADP + phosphate + L-glutamine.

Enzyme regulation

The activity of this enzyme is controlled by adenylation under conditions of abundant glutamine. The fully adenylated enzyme complex is inactive By similarity.

Subunit structure

Oligomer of 12 subunits arranged in the form of two hexagons.

Subcellular location

Cytoplasm.

Miscellaneous

Two forms of glutamine synthetase (GSI and GSII) can be found in this nitrogen fixing bacteria, GSI is a typical prokaryotic glutamine synthetase whereas GSII is similar to the eukaryotic enzyme.

Sequence similarities

Belongs to the glutamine synthetase family.

Ontologies

Keywords
   Biological processNitrogen fixation
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
Gene Ontology (GO)
   Biological_processglutamine biosynthetic process

Inferred from electronic annotation. Source: InterPro

nitrogen fixation

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

glutamate-ammonia ligase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 469469Glutamine synthetase 1
PRO_0000153223

Amino acid modifications

Modified residue3981O-AMP-tyrosine By similarity

Sequences

Sequence LengthMass (Da)Tools
P09826 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: A1E158ECD0970FBC

FASTA46952,233
        10         20         30         40         50         60 
MATASEILKQ IKENDVKFVD LRFTDRRASL QHVTMDVVCV DEDMFADGVM FDGFSIGGWK 

        70         80         90        100        110        120 
AINESDMVLM PDTETVHMDP FFAQSTMVIV CDILDPVSGE AYNRDRRGTA KKAEAYLKAS 

       130        140        150        160        170        180 
GIGDTVFVGR EAEFFVFDDV KYKADPYNTG FKLDSTELPS NDDTDYETGN LGHRPRVKGG 

       190        200        210        220        230        240 
YFPVPPVDSA QDMRSEMLTV LSEMGVVVEK HHHEVAAAQH DTLVRNADEL GIKFKMQIYK 

       250        260        270        280        290        300 
YVVHQVANAY GKTATFMPKP IFGDNGSGMH VHQSIWKGGK PTFAGDEYAG LSESCLFYIG 

       310        320        330        340        350        360 
GIIKHAKAIN AFTNPSTNSY KRFVPGYEAP VLLAYSARNR SASCRIPFGS NPKAKRVEVR 

       370        380        390        400        410        420 
FPDPTANPYL AFAAMLMAGL DGIKNKIHPG KAMDKDLYDL PPKELKKIPT VCGSLRQALE 

       430        440        450        460 
SLDKDRKFLT AGGVFDDDQI DAFIELKMAE VMRFEMTPHP VEYDMYYSA 

« Hide

References

[1]"Tight linkage of glnA and a putative regulatory gene in Rhizobium leguminosarum."
Colonna-Romano S., Riccio A., Guida M., Defez R., Lamberti A., Iaccarino M., Arnold W., Priefer U., Puehler A.
Nucleic Acids Res. 15:1951-1964(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: RCC1001.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X04880 Genomic DNA. Translation: CAA28569.1.
PIRAJZRQL. A26567.

3D structure databases

ProteinModelPortalP09826.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

ProMEXP09826.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.10.20.70. 1 hit.
3.30.590.10. 1 hit.
InterProIPR008147. Gln_synt_beta.
IPR014746. Gln_synth/guanido_kin_cat_dom.
IPR008146. Gln_synth_cat_dom.
IPR027303. Gln_synth_gly_rich_site.
IPR004809. Gln_synth_I.
IPR001637. Gln_synth_I_adenylation_site.
[Graphical view]
PfamPF00120. Gln-synt_C. 1 hit.
PF03951. Gln-synt_N. 1 hit.
[Graphical view]
SUPFAMSSF54368. SSF54368. 1 hit.
TIGRFAMsTIGR00653. GlnA. 1 hit.
PROSITEPS00182. GLNA_ADENYLATION. 1 hit.
PS00181. GLNA_ATP. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLNA1_RHILV
AccessionPrimary (citable) accession number: P09826
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: February 19, 2014
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families